| Title: | A Peptide Derived from Phosphoinositide 3-kinase Inhibits Endocytosis and Influenza Virus Infection |
| Authors: | Fujioka, Yoichiro Browse this author →KAKEN DB |
| Satoh, Aya O. Browse this author |
| Horiuchi, Kosui Browse this author |
| Fujioka, Mari Browse this author |
| Tsutsumi, Kaori Browse this author →KAKEN DB |
| Sasaki, Junko Browse this author →KAKEN DB |
| Nepal, Prabha Browse this author |
| Kashiwagi, Sayaka Browse this author |
| Paudel, Sarad Browse this author →KAKEN DB |
| Nishide, Shinya Browse this author →KAKEN DB |
| Nanbo, Asuka Browse this author →KAKEN DB |
| Sasaki, Takehiko Browse this author →KAKEN DB |
| Ohba, Yusuke Browse this author →KAKEN DB |
| Keywords: | signal transduction |
| endocytosis |
| endosome |
| imaging |
| influenza virus |
| Issue Date: | 2019 |
| Publisher: | Japan Society for Cell Biology |
| Journal Title: | Cell structure and function |
| Volume: | 44 |
| Issue: | 1 |
| Start Page: | 61 |
| End Page: | 74 |
| Publisher DOI: | 10.1247/csf.19001 |
| Abstract: | Endocytosis mediates the internalization and ingestion of a variety of endogenous or exogenous substances, including virus particles, under the control of intracellular signaling pathways. We have previously reported that the complex formed between the small GTPase Ras and phosphoinositide 3-kinase (PI3K) translocates from the plasma membrane to endosomes, signaling from which thereby regulates clathrin-independent endocytosis, endosome maturation, influenza virus internalization, and infection. However, the molecular mechanism by which the Ras-PI3K complex is recruited to endosomes remains unclear. Here, we have identified the amino acid sequence responsible for endosomal localization of the Ras-PI3K complex. PI3K lacking this sequence failed to translocate to endosomes, and expression of the peptide comprising this PI3K-derived sequence inhibited clathrin-independent endocytosis, influenza virus internalization, and infection. Moreover, treatment of cells with this peptide in an arginine-rich, cell-penetrating form successfully suppressed influenza virus infection in vitro and ex vivo, making this peptide a potential therapeutic agent against influenza virus infection. |
| Rights: | http://creativecommons.org/licenses/BY/4.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/76512 |
| Appears in Collections: | 医学院・医学研究院 (Graduate School of Medicine / Faculty of Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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